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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Zinc folds the N-terminal domain of HIV-1 integrase, promotes multimerization, and enhances catalytic activity
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Zinc folds the N-terminal domain of HIV-1 integrase, promotes multimerization, and enhances catalytic activity

机译:锌折叠HIV-1整合酶的N末端结构域,促进多聚化并增强催化活性

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摘要

The N-terminal domain of HIV-1 integrase contains a pair of His and Cys residues (the HHCC motif) that are conserved among retroviral integrases. Although His and Cys residues are often involved in binding zinc, the HHCC motif does not correspond to any recognized class of zinc binding domain. We have investigated the binding of zinc to HIV-1 integrase protein and find that it binds zinc with a stoichiometry of one zinc per integrase monomer. Analysis of zinc binding to deletion derivatives of integrase locates the binding site to the N-terminal domain.
机译:HIV-1整合酶的N端结构域包含一对在逆转录病毒整合中保守的His和Cys残基(HHCC基序)。尽管His和Cys残基经常参与结合锌,但HHCC基序并不对应于任何公认的锌结合结构域类别。我们研究了锌与HIV-1整合酶蛋白的结合,发现它与锌的化学计量比为每整合酶单体结合一个锌。锌与整合酶缺失衍生物的结合分析将结合位点定位于N-末端结构域。

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